SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q1Q8J9

- FADB_PSYCK

UniProt

Q1Q8J9 - FADB_PSYCK

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Fatty acid oxidation complex subunit alpha
Gene
fadB, Pcryo_2227
Organism
Psychrobacter cryohalolentis (strain K5)
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

Functioni

Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate By similarity.UniRule annotation

Catalytic activityi

(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH.UniRule annotation
(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O.UniRule annotation
(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA.UniRule annotation
(3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei120 – 1201Important for catalytic activity By similarity
Sitei140 – 1401Important for catalytic activity By similarity
Binding sitei298 – 2981Substrate By similarity
Binding sitei326 – 3261NAD; via amide nitrogen By similarity
Binding sitei345 – 3451NAD By similarity
Binding sitei409 – 4091NAD By similarity
Active sitei452 – 4521For 3-hydroxyacyl-CoA dehydrogenase activity By similarity
Binding sitei455 – 4551NAD By similarity
Binding sitei502 – 5021Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi402 – 4043NAD By similarity
Nucleotide bindingi429 – 4313NAD By similarity

GO - Molecular functioni

  1. 3-hydroxyacyl-CoA dehydrogenase activity Source: UniProtKB-HAMAP
  2. 3-hydroxybutyryl-CoA epimerase activity Source: UniProtKB-HAMAP
  3. coenzyme binding Source: InterPro
  4. dodecenoyl-CoA delta-isomerase activity Source: UniProtKB-HAMAP
  5. enoyl-CoA hydratase activity Source: UniProtKB-HAMAP
Complete GO annotation...

GO - Biological processi

  1. fatty acid beta-oxidation Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Lyase, Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid degradation, Lipid metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciPCRY335284:GHE9-2271-MONOMER.
UniPathwayiUPA00659.

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid oxidation complex subunit alpha
Including the following 2 domains:
Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC:4.2.1.17, EC:5.1.2.3, EC:5.3.3.8)
3-hydroxyacyl-CoA dehydrogenase (EC:1.1.1.35)
Gene namesi
Name:fadB
Ordered Locus Names:Pcryo_2227
OrganismiPsychrobacter cryohalolentis (strain K5)
Taxonomic identifieri335284 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaePsychrobacter
ProteomesiUP000002425: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. fatty acid beta-oxidation multienzyme complex Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 719719Fatty acid oxidation complex subunit alphaUniRule annotation
PRO_0000255844Add
BLAST

Interactioni

Subunit structurei

Heterotetramer of two alpha chains (FadB) and two beta chains (FadA) By similarity.

Protein-protein interaction databases

STRINGi335284.Pcryo_2227.

Structurei

3D structure databases

ProteinModelPortaliQ1Q8J9.
SMRiQ1Q8J9. Positions 1-717.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 190190Enoyl-CoA hydratase/isomerase By similarity
Add
BLAST
Regioni313 – 7194073-hydroxyacyl-CoA dehydrogenase By similarity
Add
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.
In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.

Phylogenomic databases

eggNOGiCOG1250.
HOGENOMiHOG000261344.
KOiK01825.
OMAiAKGMVMQ.
OrthoDBiEOG6M9F0M.

Family and domain databases

Gene3Di1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 1 hit.
HAMAPiMF_01621. FadB.
InterProiIPR006180. 3-OHacyl-CoA_DH_CS.
IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR013328. DH_multihelical.
IPR012799. FadB.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00725. 3HCDH. 1 hit.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 2 hits.
SSF52096. SSF52096. 1 hit.
TIGRFAMsiTIGR02437. FadB. 1 hit.
PROSITEiPS00067. 3HCDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q1Q8J9-1 [UniParc]FASTAAdd to Basket

« Hide

MVYQGNRITV TMLEDGIANM QYNAENESVN KFDTETNKQF AEVVNALEKA    50
DDIKGLIVTS SKGVFIAGAD ITEFVASFKQ SEEEIKDWVI NINDAFNRFE 100
DLPFPKVAAI NGAALGGGCE MTLVCEYRVM SDKAIIGLPE TQLGIFPGFG 150
GTVRSTRVIG IDNALELIAT GTPKKALDAL KLGLVDATVA ADDLQDAAID 200
LVKKCISDEL DWQAKREEKL VPVKLNQLEQ AMAFNSAKGM IFAKANPKQY 250
PAPALAIAAI EKHVNLPRDK AIEVEAAGFA KAAKTPQAES LVGLFLSDQL 300
VKKLAKQHSK KAHDINEAAV LGAGIMGGGI AYQAASKGLP IIMKDIKSEQ 350
LDLGMGEASK LLGKMVDRGK ITPAKMGETL SRIRPTLNYG DFAETDIVIE 400
AVVENPNVKR AVLKEVEGLV KDDCILASNT STISITFLAE ALERPENFVG 450
MHFFNPVNRM PLVEVIRGEK SSEEAISTTV ALATKMGKVP VVVNDCPGFL 500
VNRVLFPYFG AFDLLLKQGA DFAHVDKVME KFGWPMGPAY LIDVVGLDTG 550
VHGAEVMAEG FPDRMKPDYK GAIEHLYENK RLGQKNGVGF YKYEMDKRGK 600
PKKVADEATY ELLKTTTDSD KQTFEDQAII DRTMLAFCNE TVRCLEDNIV 650
STPSEADMAM IMGVGFPPFR GGPCRYIDQM GLDNYLALCE KYAYLGKAYE 700
APQKIRDMAA AGETFYATA 719
Length:719
Mass (Da):78,378
Last modified:May 16, 2006 - v1
Checksum:i0A15859CAFCD9966
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000323 Genomic DNA. Translation: ABE76004.1.
RefSeqiYP_581488.1. NC_007969.1.

Genome annotation databases

EnsemblBacteriaiABE76004; ABE76004; Pcryo_2227.
GeneIDi4033840.
KEGGipcr:Pcryo_2227.
PATRICi23064087. VBIPsyCry128170_2356.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000323 Genomic DNA. Translation: ABE76004.1 .
RefSeqi YP_581488.1. NC_007969.1.

3D structure databases

ProteinModelPortali Q1Q8J9.
SMRi Q1Q8J9. Positions 1-717.
ModBasei Search...

Protein-protein interaction databases

STRINGi 335284.Pcryo_2227.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABE76004 ; ABE76004 ; Pcryo_2227 .
GeneIDi 4033840.
KEGGi pcr:Pcryo_2227.
PATRICi 23064087. VBIPsyCry128170_2356.

Phylogenomic databases

eggNOGi COG1250.
HOGENOMi HOG000261344.
KOi K01825.
OMAi AKGMVMQ.
OrthoDBi EOG6M9F0M.

Enzyme and pathway databases

UniPathwayi UPA00659 .
BioCyci PCRY335284:GHE9-2271-MONOMER.

Family and domain databases

Gene3Di 1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 1 hit.
HAMAPi MF_01621. FadB.
InterProi IPR006180. 3-OHacyl-CoA_DH_CS.
IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR013328. DH_multihelical.
IPR012799. FadB.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
Pfami PF00725. 3HCDH. 1 hit.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view ]
SUPFAMi SSF48179. SSF48179. 2 hits.
SSF52096. SSF52096. 1 hit.
TIGRFAMsi TIGR02437. FadB. 1 hit.
PROSITEi PS00067. 3HCDH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Complete sequence of chromosome of Psychrobacter cryohalolentis K5."
    US DOE Joint Genome Institute
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Sims D.R., Gilna P., Schmutz J.
    , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Richardson P.
    Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K5.

Entry informationi

Entry nameiFADB_PSYCK
AccessioniPrimary (citable) accession number: Q1Q8J9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: May 16, 2006
Last modified: June 11, 2014
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi